LOX2_ORYSJ
ID LOX2_ORYSJ Reviewed; 870 AA.
AC P29250; Q10D65; Q7Y1F4;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Linoleate 9S-lipoxygenase 2;
DE EC=1.13.11.58;
DE AltName: Full=Lipoxygenase 2;
DE AltName: Full=Lipoxygenase L-2;
GN Name=LOX1.1; OrderedLocusNames=Os03g0738600, LOC_Os03g52860;
GN ORFNames=OsJ_12500 {ECO:0000312|EMBL:EAZ28520.1}, OSJNBa0057G07.15;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=cv. Nipponbare; TISSUE=Seedling;
RX PubMed=1597177; DOI=10.1111/j.1432-1033.1992.tb16931.x;
RA Ohta H., Shirano Y., Tanaka K., Morita Y., Shibata D.;
RT "cDNA cloning of rice lipoxygenase L-2 and characterization using an active
RT enzyme expressed from the cDNA in Escherichia coli.";
RL Eur. J. Biochem. 206:331-336(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16109971; DOI=10.1101/gr.3869505;
RG The rice chromosome 3 sequencing consortium;
RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA Jin W., Lee H.R., Jiang J., Jackson S.;
RT "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT and diverged grass species.";
RL Genome Res. 15:1284-1291(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
CC -!- FUNCTION: Plant lipoxygenase may be involved in a number of diverse
CC aspects of plant physiology including growth and development, pest
CC resistance, and senescence or responses to wounding. Catalyzes the
CC hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene
CC structure. {ECO:0000269|PubMed:1597177}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoate + O2 = (9S)-hydroperoxy-(10E,12Z)-
CC octadecadienoate; Xref=Rhea:RHEA:30291, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:60955; EC=1.13.11.58;
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00726};
CC Note=Binds 1 Fe cation per subunit. Iron is tightly bound.
CC {ECO:0000255|PROSITE-ProRule:PRU00726};
CC -!- PATHWAY: Lipid metabolism; oxylipin biosynthesis. {ECO:0000255|PROSITE-
CC ProRule:PRU00726}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00726}.
CC -!- SIMILARITY: Belongs to the lipoxygenase family. {ECO:0000305}.
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DR EMBL; X64396; CAA45738.1; -; mRNA.
DR EMBL; AC117988; AAP44707.1; -; Genomic_DNA.
DR EMBL; DP000009; ABF98775.1; -; Genomic_DNA.
DR EMBL; AP008209; BAF13126.1; -; Genomic_DNA.
DR EMBL; AP014959; BAS86291.1; -; Genomic_DNA.
DR EMBL; CM000140; EAZ28520.1; -; Genomic_DNA.
DR EMBL; AK073529; BAG93501.1; -; mRNA.
DR PIR; S23454; S23454.
DR RefSeq; XP_015629809.1; XM_015774323.1.
DR AlphaFoldDB; P29250; -.
DR SMR; P29250; -.
DR STRING; 4530.OS03T0738600-01; -.
DR PaxDb; P29250; -.
DR PRIDE; P29250; -.
DR EnsemblPlants; Os03t0738600-01; Os03t0738600-01; Os03g0738600.
DR GeneID; 4334049; -.
DR Gramene; Os03t0738600-01; Os03t0738600-01; Os03g0738600.
DR KEGG; osa:4334049; -.
DR eggNOG; ENOG502QQSP; Eukaryota.
DR HOGENOM; CLU_004282_0_0_1; -.
DR InParanoid; P29250; -.
DR OMA; FDSTPDE; -.
DR OrthoDB; 385042at2759; -.
DR BRENDA; 1.13.11.58; 4460.
DR UniPathway; UPA00382; -.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000007752; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
DR Genevisible; P29250; OS.
DR GO; GO:0005737; C:cytoplasm; IDA:Gramene.
DR GO; GO:0016165; F:linoleate 13S-lipoxygenase activity; IDA:Gramene.
DR GO; GO:1990136; F:linoleate 9S-lipoxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IBA:GO_Central.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0034440; P:lipid oxidation; IBA:GO_Central.
DR GO; GO:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0051707; P:response to other organism; IDA:Gramene.
DR GO; GO:0009611; P:response to wounding; IDA:Gramene.
DR CDD; cd01751; PLAT_LH2; 1.
DR Gene3D; 4.10.372.10; -; 1.
DR InterPro; IPR000907; LipOase.
DR InterPro; IPR013819; LipOase_C.
DR InterPro; IPR036226; LipOase_C_sf.
DR InterPro; IPR020834; LipOase_CS.
DR InterPro; IPR020833; LipOase_Fe_BS.
DR InterPro; IPR001246; LipOase_plant.
DR InterPro; IPR042057; Lipoxy_PLAT/LH2.
DR InterPro; IPR027433; Lipoxygenase_dom_3.
DR InterPro; IPR001024; PLAT/LH2_dom.
DR InterPro; IPR036392; PLAT/LH2_dom_sf.
DR PANTHER; PTHR11771; PTHR11771; 1.
DR Pfam; PF00305; Lipoxygenase; 1.
DR Pfam; PF01477; PLAT; 1.
DR PRINTS; PR00087; LIPOXYGENASE.
DR PRINTS; PR00468; PLTLPOXGNASE.
DR SMART; SM00308; LH2; 1.
DR SUPFAM; SSF48484; SSF48484; 1.
DR SUPFAM; SSF49723; SSF49723; 1.
DR PROSITE; PS00711; LIPOXYGENASE_1; 1.
DR PROSITE; PS00081; LIPOXYGENASE_2; 1.
DR PROSITE; PS51393; LIPOXYGENASE_3; 1.
DR PROSITE; PS50095; PLAT; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Dioxygenase; Fatty acid biosynthesis; Fatty acid metabolism;
KW Iron; Lipid biosynthesis; Lipid metabolism; Metal-binding; Oxidoreductase;
KW Oxylipin biosynthesis; Reference proteome.
FT CHAIN 1..870
FT /note="Linoleate 9S-lipoxygenase 2"
FT /id="PRO_0000220708"
FT DOMAIN 32..158
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DOMAIN 161..870
FT /note="Lipoxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT REGION 203..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..241
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 525
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 530
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 716
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 720
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 870
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT CONFLICT 40..41
FT /note="DG -> ER (in Ref. 1; CAA45738)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="P -> A (in Ref. 1; CAA45738)"
FT /evidence="ECO:0000305"
FT CONFLICT 336
FT /note="Missing (in Ref. 1; CAA45738)"
FT /evidence="ECO:0000305"
FT CONFLICT 385..387
FT /note="RSR -> EP (in Ref. 1; CAA45738)"
FT /evidence="ECO:0000305"
FT CONFLICT 464
FT /note="Missing (in Ref. 1; CAA45738)"
FT /evidence="ECO:0000305"
FT CONFLICT 492..500
FT /note="RGGTGAGAV -> AAAPAPAL (in Ref. 1; CAA45738)"
FT /evidence="ECO:0000305"
FT CONFLICT 566
FT /note="A -> G (in Ref. 1; CAA45738)"
FT /evidence="ECO:0000305"
FT CONFLICT 587..588
FT /note="KH -> ND (in Ref. 1; CAA45738)"
FT /evidence="ECO:0000305"
FT CONFLICT 617..619
FT /note="AVP -> RT (in Ref. 1; CAA45738)"
FT /evidence="ECO:0000305"
FT CONFLICT 644..646
FT /note="WHA -> CTP (in Ref. 1; CAA45738)"
FT /evidence="ECO:0000305"
FT CONFLICT 700..701
FT /note="EL -> DV (in Ref. 1; CAA45738)"
FT /evidence="ECO:0000305"
FT CONFLICT 740
FT /note="P -> A (in Ref. 1; CAA45738)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 870 AA; 97184 MW; 63344755867DA6E0 CRC64;
MLGGIIGGLT GNKNARLKGS LVLMRKNALD INDFGATVID GISEFLGRGV TCQLVSSSLV
DPNNGNRGRV GTEASLEQWL TSLPSLTTGE SKFGVTFEWE VEKMGIPGAI IVKNNHAAEF
FLKTITLDNV PGHGAVVFVA NSWIYPASKY RYNRVFFSND TSLPSKMPAA LKPYRDDELR
NLRGDDQQGP YQEHDRVYRY DVYNDLGEPD SGNPRPVLGG SPDRPYPRRG RTGRKPTKTD
PTAESRLSLL ENIYVPRDER FGHLKMADFL GYSIKALVDG IVPAIRTYVD LTPGEFDSFK
DILKLYEGGL KLPSIPALEE LRKRFPLQLV KDLIPAGGDY LLKLPMPHVI REDKKAWMTD
DEFAREILAG VNPMVIARLT EFPPRSRLDP ARYGDQTSTI TAAHVERGLE GLTVQQAIDG
NLLYVVDHHD HFMPYLLDIN SLDDNFIYAT RTLLFLRGDG TLAPLAIELS LPHLQDDGLI
TARSTVYTPA ARGGTGAGAV EWWVWQLAKA YVNVNDYCWH QLISHWLNTH AVMEPFVIAT
NRQLSVAHPV HKLLLPHYRD TMTINALARQ TLINGGGIFE MTVFPRKHAL AMSSAFYKDW
SFADQALPDD LVKRGVAVPD PASPYKVRLL IEDYPYANDG LAVWHAIEQW ATEYLAIYYP
NDGVLQGDAE LQAWWKEVRE VGHGDIKDAT WWPEMKTVAE LVKACATIIW IGSALHAAVN
FGQYPYAGYL PNRPSVSRRP MPEPGTKEYD ELARDPEKVF VRTITKQMQA IVGISLLEIL
SKHSSDEVYL GQRDTPEWTS DAKALEAFKR FGARLTEIES RVVAMNKDPH RKNRVGPTNF
PYTLLYPNTS DLKGDAAGLS ARGIPNSISI
